Assisting the reactivation of guanidine hydrochloride-denatured aminoacylase by hydroxypropyl cyclodextrins.

Biophysical Journal
Sung-Hye KimYong-Bin Yan

Abstract

Cyclodextrin is a water-soluble circular oligosaccharide with a cylinder shape characterized by exterior hydrophilic rims and an interior hydrophobic cavity, which makes it an ideal additive to prevent proteins from aggregating during refolding. In this research, three hydroxypropyl cyclodextrins (HPCDs), HP-alpha-, beta-, and gamma-CD, were used to investigate the molecular mechanism of their effects on assisting aminoacylase refolding. The aggregation and reactivation experiments suggested that at moderate concentrations, HPCDs could suppress aggregation and assist aminoacylase refolding in a concentration-dependent manner, and HP-beta-CD was the most efficient of the three HPCDs. Low concentrations of HP-alpha-CD and high concentrations of HP-gamma-CD promoted off-pathway aggregation. Spectroscopic studies indicated that the hydrophobic exposure of the unstructured species in the refolded solutions was gradually reduced by the three HPCDs with the efficiency HP-beta-CD > HP-gamma-CD > HP-alpha-CD. Furthermore, the fast phase of aminoacylase reactivation was slowed down by the addition of 75 mM HP-beta- and gamma-CD, but no significant effect was observed for HP-alpha-CD. The dissimilarity in the effects of the three HPCDs su...Continue Reading

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Citations

Jun 4, 2008·The Protein Journal·Mohammad Ali Esmaeili, Razieh Yazdanparast
Jul 27, 2010·Journal of Ocular Pharmacology and Therapeutics : the Official Journal of the Association for Ocular Pharmacology and Therapeutics·Hong ZhangHao Cui
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Apr 3, 2016·Chemistry, an Asian Journal·Valentina Oliveri, Graziella Vecchio
Jul 11, 2006·International Journal of Biological Macromolecules·Sung-Hye KimYong-Bin Yan

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